Targeting Insulin Amyloid Assembly by Aminosugars and Their Derivatives

Title: Targeting Insulin Amyloid Assembly by Aminosugars and Their Derivatives

Volume: 18 Issue: 6

Author(s): V. Nagaveni, M. Sravani, S. Prabhakar, B. Sreedhar and M. Vairamani

Affiliation:

Keywords: Insulin, amyloid, amino sugars, transmission electron microscopy, mass spectrometry, N-acetylhexosamines, fibrilsInsulin, amyloid, amino sugars, transmission electron microscopy, mass spectrometry, N-acetylhexosamines, fibrils

Abstract: The use of small carbohydrates that stabilize proteins from misfolding is important from pharmaceutical point of view. We have investigated the role of small isomeric amino sugars on the in vitro aggregation of insulin amyloid. Using mass spectrometry, we screened 6 isomeric aminosugars for their role on inhibition of insulin amyloid formation and the results were compared with transmission electron microscopy imaging. We found that three N-acetylamino sugars promote insulin fibril formation. Among three isomeric aminosugars studied, only galactosamine showed few fibrils whereas other two isomers showed enhanced fibrils. The results demonstrated here may contribute to future designing of small amine derivatised galactose sugars as amyloid inhibitors and understanding their action.

Cite this article as:

Nagaveni V., Sravani M., Prabhakar S., Sreedhar B. and Vairamani M., Targeting Insulin Amyloid Assembly by Aminosugars and Their Derivatives, Protein & Peptide Letters 2011; 18 (6) . https://dx.doi.org/10.2174/092986611795222687